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Nitroglycerin metabolism by Phanerochaete chrysosporium: evidence for nitric oxide and nitrite formation.

Identifieur interne : 000F15 ( Main/Corpus ); précédent : 000F14; suivant : 000F16

Nitroglycerin metabolism by Phanerochaete chrysosporium: evidence for nitric oxide and nitrite formation.

Auteurs : D. Servent ; C. Ducrocq ; Y. Henry ; A. Guissani ; M. Lenfant

Source :

RBID : pubmed:1648402

English descriptors

Abstract

We have demonstrated that a filamentous fungus Phanerochaete chrysosporium converts glyceryl trinitrate (GTN) into its di- and mononitrate derivatives concurrently with the formation of nitric oxide detected by electron paramagnetic resonance (EPR), and the formation of nitrite. The metabolisms of nitrite and nitrate by the fungus are evaluated and taken into account when considering GTN degradation. Lack of evidence for nitrate formation from GTN suggests that an esterase-type activity is not involved. Furthermore, the kinetics of appearance of the hemoprotein-NO and non-heme protein-NO (FeS-NO) complexes indicate that an enzymatic process producing NO directly from GTN may be involved concurrently with a glutathione transferase-like system.

DOI: 10.1016/0304-4165(91)90170-l
PubMed: 1648402

Links to Exploration step

pubmed:1648402

Le document en format XML

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<name sortKey="Servent, D" sort="Servent, D" uniqKey="Servent D" first="D" last="Servent">D. Servent</name>
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<name sortKey="Ducrocq, C" sort="Ducrocq, C" uniqKey="Ducrocq C" first="C" last="Ducrocq">C. Ducrocq</name>
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<name sortKey="Henry, Y" sort="Henry, Y" uniqKey="Henry Y" first="Y" last="Henry">Y. Henry</name>
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<name sortKey="Guissani, A" sort="Guissani, A" uniqKey="Guissani A" first="A" last="Guissani">A. Guissani</name>
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<name sortKey="Lenfant, M" sort="Lenfant, M" uniqKey="Lenfant M" first="M" last="Lenfant">M. Lenfant</name>
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<term>Aerobiosis (MeSH)</term>
<term>Chromatography, High Pressure Liquid (MeSH)</term>
<term>Chrysosporium (metabolism)</term>
<term>Colorimetry (MeSH)</term>
<term>Electron Spin Resonance Spectroscopy (MeSH)</term>
<term>Glutathione Transferase (metabolism)</term>
<term>Hemeproteins (metabolism)</term>
<term>Models, Chemical (MeSH)</term>
<term>Nitric Oxide (metabolism)</term>
<term>Nitrites (metabolism)</term>
<term>Nitroglycerin (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Glutathione Transferase</term>
<term>Hemeproteins</term>
<term>Nitric Oxide</term>
<term>Nitrites</term>
<term>Nitroglycerin</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Chrysosporium</term>
</keywords>
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<term>Aerobiosis</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Colorimetry</term>
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<div type="abstract" xml:lang="en">We have demonstrated that a filamentous fungus Phanerochaete chrysosporium converts glyceryl trinitrate (GTN) into its di- and mononitrate derivatives concurrently with the formation of nitric oxide detected by electron paramagnetic resonance (EPR), and the formation of nitrite. The metabolisms of nitrite and nitrate by the fungus are evaluated and taken into account when considering GTN degradation. Lack of evidence for nitrate formation from GTN suggests that an esterase-type activity is not involved. Furthermore, the kinetics of appearance of the hemoprotein-NO and non-heme protein-NO (FeS-NO) complexes indicate that an enzymatic process producing NO directly from GTN may be involved concurrently with a glutathione transferase-like system.</div>
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<Title>Biochimica et biophysica acta</Title>
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<AbstractText>We have demonstrated that a filamentous fungus Phanerochaete chrysosporium converts glyceryl trinitrate (GTN) into its di- and mononitrate derivatives concurrently with the formation of nitric oxide detected by electron paramagnetic resonance (EPR), and the formation of nitrite. The metabolisms of nitrite and nitrate by the fungus are evaluated and taken into account when considering GTN degradation. Lack of evidence for nitrate formation from GTN suggests that an esterase-type activity is not involved. Furthermore, the kinetics of appearance of the hemoprotein-NO and non-heme protein-NO (FeS-NO) complexes indicate that an enzymatic process producing NO directly from GTN may be involved concurrently with a glutathione transferase-like system.</AbstractText>
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